Two-Dimensional Electrophoresis of Pseudocholinesterase Components in Normal Human Serum

Nature ◽  
1962 ◽  
Vol 196 (4861) ◽  
pp. 1296-1298 ◽  
Author(s):  
H. HARRIS ◽  
D. A. HOPKINSON ◽  
E. B. ROBSON
Keyword(s):  
Human Serum ◽  
Normal Human Serum ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Normal Human ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis analysis of human serum proteins during the acute-phase response

1992 ◽  
Vol 13 (1) ◽  
pp. 743-746 ◽  
Author(s):  
Luca Bini ◽  
Barbara Magi ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
Vitaliano Pallini
Keyword(s):  
Human Serum ◽  
Acute Phase ◽  
Acute Phase Response ◽  
Serum Proteins ◽  
Phase Response ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Human Serum Proteins

Muscle protein analysis. II. Two-dimensional electrophoresis of normal and diseased human skeletal muscle.

1980 ◽  
Vol 26 (8) ◽  
pp. 1152-1155 ◽  
Author(s):  
C S Giometti ◽  
M Bárány ◽  
M J Danon ◽  
N G Anderson
Keyword(s):  
Muscle Protein ◽  
Human Muscle ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Two Dimensional ◽  
Normal Muscle ◽  
Two Dimensional Electrophoresis ◽  
Three Samples ◽  
Normal Human ◽  
Dimensional Electrophoresis

Abstract We used high-resolution two-dimensional electrophoresis to analyze the major proteins of normal and pathological human-muscle samples. The normal human-muscle pattern contains four myosin light chains: three that co-migrate with the myosin light chains from rabbit fast muscle (extensor digitorum longus), and one that co-migrates with the light chain 2 from rabbit slow muscle (soleus). Of seven Duchenne muscular dystrophy samples, four yielded patterns with decreased amounts of actin and myosin relative to normal muscle, while three samples gave patterns comparable to that for normal muscle. Six samples from patients with myotonic dystrophy also gave normal patterns. In nemaline rod myopathy, in contrast, the pattern was deficient in two of the fast-type myosin light chains.

The Two-Dimensional Electrophoresis of Human Serum DNA-Binding Proteins

1979 ◽  
Vol 7 (5) ◽  
pp. 1089-1090 ◽  
Author(s):  
ANNE E. HUGHES ◽  
W. SIDNEY B. LOWRY ◽  
J. ALAN HILL ◽  
R. JEREMY H. DAVIES
Keyword(s):  
Dna Binding ◽  
Human Serum ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Serum Dna ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment

1995 ◽  
Vol 16 (1) ◽  
pp. 1190-1192 ◽  
Author(s):  
Barbara Magi ◽  
Barbara Marzocchi ◽  
Luca Bini ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Two Dimensional ◽  
Therapeutic Treatment ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Human Serum Proteins

The human serum proteome: Display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins

PROTEOMICS ◽  
2003 ◽  
Vol 3 (7) ◽  
pp. 1345-1364 ◽  
Author(s):  
Rembert Pieper ◽  
Christine L. Gatlin ◽  
Anthony J. Makusky ◽  
Paul S. Russo ◽  
Courtney R. Schatz ◽  
...  
Keyword(s):  
Human Serum ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Serum Proteome ◽  
Dimensional Electrophoresis

Lymphocyte, monocyte, and granulocyte proteins compared by use of two-dimensional electrophoresis.

1982 ◽  
Vol 28 (4) ◽  
pp. 1062-1066 ◽  
Author(s):  
M A Gemmell ◽  
N L Anderson
Keyword(s):  
Cultured Cells ◽  
Normal Skin ◽  
Specific Marker ◽  
Two Dimensional ◽  
Cell Type ◽  
Two Dimensional Electrophoresis ◽  
Marker Proteins ◽  
Normal Human ◽  
Normal Skin Fibroblast ◽  
Dimensional Electrophoresis

Abstract We compared cellular proteins from normal human blood lymphocytes, monocytes and granulocytes, using high-resolution two-dimensional electrophoresis. The leukocytes were isolated from peripheral blood by centrifugation on density step gradients (yielding a fraction of purified granulocytes and a lymphocyte/monocyte mixture) and monocytes were subsequently separated from lymphocytes by virtue of their adherence to plastic. Wright-stained smears indicated that each of the three resulting fractions was 90 to 95% pure. The cells were labeled with [35S]methionine after various intervals in culture, then solubilized and analyzed by two-dimensional electrophoresis. Although most proteins in each cell type are common to all three, there are nevertheless several specific marker proteins that distinguish one cell type from another. We also examined the appearance of these markers in three lines of cultured cells from humans (GM607, a B-lymphoblastoid line; HL-60, a promyelocytic leukemic line; and 1494, a normal skin fibroblast).

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